Recombinant Human IDH2, N-His

Description of Recombinant Human IDH2, N-His

Introduction

Recombinant Human IDH2 (Isocitrate Dehydrogenase 2) is a protein that plays a crucial role in cellular metabolism. It is a key enzyme in the citric acid cycle, also known as the Krebs cycle, which is responsible for the production of energy in the form of ATP. In recent years, there has been a growing interest in studying the structure, activity, and applications of recombinant human IDH2. In this article, we will discuss the various aspects of this protein in detail.

Structure of Recombinant Human IDH2

Recombinant Human IDH2 is a 452 amino acid protein with a molecular weight of approximately 51 kDa. It is composed of three distinct domains: the N-terminal domain, the catalytic domain, and the C-terminal domain. The N-terminal domain is responsible for binding to the substrate, while the catalytic domain contains the active site where the isocitrate oxidation takes place. The C-terminal domain is involved in the regulation of enzyme activity.

The crystal structure of recombinant human IDH2 has been extensively studied, and it has been found to be highly similar to that of other isocitrate dehydrogenase enzymes. It consists of a large central domain surrounded by smaller domains, which are connected by flexible linkers. The active site is located in a deep pocket within the catalytic domain, which is lined with several conserved amino acid residues that are essential for enzyme activity.

Activity of Recombinant Human IDH2

The main function of recombinant human IDH2 is to catalyze the conversion of isocitrate to alpha-ketoglutarate in the presence of NADP+. This reaction is an important step in the citric acid cycle, as it produces NADPH, which is required for various biosynthetic processes. This enzyme also plays a critical role in regulating cellular redox balance and protecting cells from oxidative stress.

Recombinant human IDH2 has been found to have a high affinity for its substrate, isocitrate, and exhibits a high turnover rate. It has also been shown to have a broad pH and temperature range for optimal activity, making it a versatile enzyme that can function in various cellular environments.

Applications of Recombinant Human IDH2

Recombinant Human IDH2 has a wide range of applications in both basic research and pharmaceutical development. One of the most significant applications of this protein is in the production of NADPH for use in various biochemical reactions. NADPH is a crucial cofactor for many enzymes involved in biosynthesis, and the availability of recombinant human IDH2 has greatly facilitated its production.

Furthermore, recombinant human IDH2 has been found to be overexpressed in various types of cancers, making it a potential target for cancer therapy. Inhibitors of this enzyme have been developed and are currently being tested in clinical trials for the treatment of IDH2-mutant acute myeloid leukemia (AML) and cholangiocarcinoma.

In addition, recombinant human IDH2 has also been used in the production of diagnostic kits for the detection of IDH2 mutations in cancer patients. These mutations have been associated with poor prognosis and can help in the early detection and treatment of certain types of cancer.

Conclusion

In conclusion, recombinant human IDH2 is a crucial enzyme involved in cellular metabolism and has various applications in both basic research and pharmaceutical development. Its well-characterized structure and high activity make it a valuable tool for the production of NADPH and the development of cancer therapies. With ongoing research, the potential applications of this protein are continuously expanding, making it an essential protein in the field of biochemistry and medicine.